Base de dados : MEDLINE
Pesquisa : D03.633.100.733.315 [Categoria DeCS]
Referências encontradas : 2813 [refinar]
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  1 / 2813 MEDLINE  
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[PMID]:27778283
[Au] Autor:Krysiak J; Breinbauer R
[Ad] Endereço:Chair of Organic Chemistry II, Technische Universität München, Lichtenbergstraße 4, 85748, Garching, Germany.
[Ti] Título:Comparative Activity-Based Flavin-Dependent Oxidase Profiling.
[So] Source:Methods Mol Biol;1491:87-99, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Activity-based protein profiling (ABPP) has become a powerful chemoproteomic technology allowing for the dissection of complex ligand-protein interactions in their native cellular environment. One of the biggest challenges for ABPP is the extension of the proteome coverage. In this chapter a new ABPP strategy dedicated to monoamine oxidases (MAO) is presented. These enzymes are representative examples of flavin-dependent oxidases, playing a crucial role in the regulation of nervous system signaling.
[Mh] Termos MeSH primário: Flavinas/metabolismo
Monoaminoxidase/metabolismo
Proteômica
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Sistema Nervoso Central/enzimologia
Sistema Nervoso Central/metabolismo
Eletroforese em Gel de Poliacrilamida
Seres Humanos
Camundongos
Transdução de Sinais
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Flavins); EC 1.4.3.4 (Monoamine Oxidase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 2813 MEDLINE  
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[PMID]:28919416
[Au] Autor:Martín Del Campo JS; Eckshtain-Levi M; Sobrado P
[Ad] Endereço:Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061, USA.
[Ti] Título:Identification of eukaryotic UDP-galactopyranose mutase inhibitors using the ThermoFAD assay.
[So] Source:Biochem Biophys Res Commun;493(1):58-63, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Aspergillus fumigatus is a human pathogen responsible for deadly infections in immune-compromised patients. A potential strategy for treating A. fumigatus infections is by targeting the biosynthesis of cell wall components, such as galactofuranase, which is absent in humans. Galactofuranose biosynthesis is initiated by the flavoenzyme UDP-galactopyranose mutase (UGM), which converts UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf). UGM requires the reduced form of the flavin for activity, which is obtained by reacting with NADPH. We aimed to identify inhibitors of UGM by screening a kinase inhibitor library using ThermoFAD, a flavin fluorescence thermal shift assay. The screening assay identified flavopiridol as a compound that increased the melting temperature of A. fumigatus UGM. Further characterization showed that flavopiridol is a non-competitive inhibitor of UGM and docking studies suggest that it binds in the active site. This compound does not inhibit the prokaryotic UGM from Mycobacteria tuberculosis.
[Mh] Termos MeSH primário: Aspergillus fumigatus/enzimologia
Avaliação Pré-Clínica de Medicamentos/métodos
Inibidores Enzimáticos/química
Flavonoides/química
Transferases Intramoleculares/antagonistas & inibidores
Piperidinas/química
Espectrometria de Fluorescência/métodos
[Mh] Termos MeSH secundário: Ativação Enzimática
Flavinas/química
Transferases Intramoleculares/análise
Mapeamento de Interação de Proteínas
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Flavins); 0 (Flavonoids); 0 (Piperidines); 45AD6X575G (alvocidib); EC 5.4.- (Intramolecular Transferases); EC 5.4.99.9 (UDP-galactopyranose mutase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


  3 / 2813 MEDLINE  
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[PMID]:28873466
[Au] Autor:Dharra R; Talwar S; Singh Y; Gupta R; Cirillo JD; Pandey AK; Kulharia M; Mehta PK
[Ad] Endereço:Centre for Biotechnology, Maharshi Dayanand University (MDU), Rohtak, India.
[Ti] Título:Rational design of drug-like compounds targeting Mycobacterium marinum MelF protein.
[So] Source:PLoS One;12(9):e0183060, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mycobacterial mel2 locus (mycobacterial enhanced infection locus, Rv1936-1941) is Mycobacterium marinum and M. tuberculosis specific, which can withstand reactive oxygen species (ROS) and reactive nitrogen species (RNS) induced stress. A library of over a million compounds was screened using in silico virtual ligand screening (VLS) to identify inhibitors against the modeled structure of MelF protein expressed by melF of mel2 locus so that M. marinum's ability to withstand ROS/RNS stress could be reduced. The top ranked 1000 compounds were further screened to identify 178 compounds to maximize the scaffold diversity by manually evaluating the interaction of each compound with the target site. M. marinum melF was cloned, expressed and purified as maltose binding protein (MBP)-tagged recombinant protein in Escherichia coli. After establishing the flavin dependent oxidoreductase activity of MelF (~ 84 kDa), the inhibitors were screened for the inhibition of enzyme activity of whole cell lysate (WCL) and the purified MelF. Amongst these, 16 compounds could significantly inhibit the enzyme activity of purified MelF. For the six best inhibitory compounds, the minimal inhibitory concentration (MIC) was determined to be 3.4-19.4 µM and 13.5-38.8 µM for M. marinum and M. tuberculosis, respectively. Similarly, the minimal bactericidal concentration (MBC) was determined to be 6.8-38.8 µM and 27-38.8 µM against M. marinum and M. tuberculosis, respectively. One compound each in combination with isoniazid (INH) also showed synergistic inhibitory effect against M. marinum and M. tuberculosis with no cytotoxicity in HeLa cells. Interestingly, these inhibitors did not display any non-specific protein-structure destabilizing effect. Such inhibitors targeting the anti-ROS/RNS machinery may facilitate the efficient killing of replicating and nonreplicating mycobacteria inside the host cells.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Bactérias/metabolismo
Desenho de Drogas
Mycobacterium marinum/efeitos dos fármacos
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/isolamento & purificação
Cromatografia Líquida de Alta Pressão
Dicroísmo Circular
Clonagem Molecular
Contagem de Colônia Microbiana
Avaliação Pré-Clínica de Medicamentos
Inibidores Enzimáticos/análise
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Flavinas/metabolismo
Cinética
Modelos Lineares
Testes de Sensibilidade Microbiana
Simulação de Acoplamento Molecular
Mycobacterium marinum/crescimento & desenvolvimento
Mycobacterium tuberculosis/efeitos dos fármacos
Mycobacterium tuberculosis/crescimento & desenvolvimento
Estrutura Secundária de Proteína
Homologia Estrutural de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Enzyme Inhibitors); 0 (Flavins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183060


  4 / 2813 MEDLINE  
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[PMID]:28821425
[Au] Autor:Karunaratne K; Luedtke N; Quinn DM; Kohen A
[Ad] Endereço:Department of Chemistry, University of Iowa, Iowa City, IA 52242, USA.
[Ti] Título:Flavin-dependent thymidylate synthase: N5 of flavin as a Methylene carrier.
[So] Source:Arch Biochem Biophys;632:11-19, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thymidylate is synthesized de novo in all living organisms for replication of genomes. The chemical transformation is reductive methylation of deoxyuridylate at C5 to form deoxythymidylate. All eukaryotes including humans complete this well-understood transformation with thymidylate synthase utilizing 6R-N -N -methylene-5,6,7,8-tetrahydrofolate as both a source of methylene and a reducing hydride. In 2002, flavin-dependent thymidylate synthase was discovered as a new pathway for de novo thymidylate synthesis. The flavin-dependent catalytic mechanism is different than thymidylate synthase because it requires flavin as a reducing agent and methylene transporter. This catalytic mechanism is not well-understood, but since it is known to be very different from thymidylate synthase, there is potential for mechanism-based inhibitors that can selectively inhibit the flavin-dependent enzyme to target many human pathogens with low host toxicity.
[Mh] Termos MeSH primário: Flavinas/química
Flavoproteínas/química
Tetra-Hidrofolatos/química
Timidilato Sintase/química
[Mh] Termos MeSH secundário: Flavinas/metabolismo
Flavoproteínas/metabolismo
Metilação
Tetra-Hidrofolatos/metabolismo
Timidina Monofosfato/biossíntese
Timidina Monofosfato/química
Timidilato Sintase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Flavins); 0 (Flavoproteins); 0 (Tetrahydrofolates); 365-07-1 (Thymidine Monophosphate); 7444-29-3 (5,10-methenyltetrahydrofolate); EC 2.1.1.45 (Thymidylate Synthase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE


  5 / 2813 MEDLINE  
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[PMID]:28784589
[Au] Autor:Adak S; Begley TP
[Ad] Endereço:Department of Chemistry, Texas A&M University, College Station, TX 77843, United States.
[Ti] Título:Flavin-N5-oxide: A new, catalytic motif in flavoenzymology.
[So] Source:Arch Biochem Biophys;632:4-10, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Flavin-N5-oxide is a recently discovered intermediate used by EncM (1,3-diketone oxidation), DszA (sulfone monooxygenase) and RutA (amide monooxygenase). This review describes the mechanism of these enzymes and proposes criteria for the identification of additional Flavin-N5-oxide dependent enzymes.
[Mh] Termos MeSH primário: Flavinas/química
Flavoproteínas/química
Oxigenases de Função Mista/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Catálise
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Flavins); 0 (Flavoproteins); EC 1.- (Mixed Function Oxygenases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE


  6 / 2813 MEDLINE  
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[PMID]:28754323
[Au] Autor:Marshall SA; Payne KAP; Leys D
[Ad] Endereço:Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester, M1 7DN, UK.
[Ti] Título:The UbiX-UbiD system: The biosynthesis and use of prenylated flavin (prFMN).
[So] Source:Arch Biochem Biophys;632:209-221, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The UbiX-UbiD system consists of the flavin prenyltransferase UbiX that produces prenylated FMN that serves as the cofactor for the (de)carboxylase UbiD. Recent developments have provided structural insights into the mechanism of both enzymes, detailing unusual chemistry in each case. The proposed reversible 1,3-dipolar cycloaddition between the cofactor and substrate serves as a model to explain many of the key UbiD family features. However, considerable variation exists in the many branches of the UbiD family tree.
[Mh] Termos MeSH primário: Carboxiliases
Dimetilaliltranstransferase
Proteínas de Escherichia coli
Escherichia coli
Flavinas
Flavoproteínas
Prenilação/fisiologia
[Mh] Termos MeSH secundário: Carboxiliases/química
Carboxiliases/genética
Carboxiliases/metabolismo
Dimetilaliltranstransferase/química
Dimetilaliltranstransferase/genética
Dimetilaliltranstransferase/metabolismo
Escherichia coli/química
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Flavinas/biossíntese
Flavinas/química
Flavinas/genética
Flavoproteínas/química
Flavoproteínas/genética
Flavoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Flavins); 0 (Flavoproteins); EC 2.5.1.1 (Dimethylallyltranstransferase); EC 4.1.1.- (3-octaprenyl-4-hydroxybenzoate carboxy-lyase); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.- (ubiX protein, E coli)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE


  7 / 2813 MEDLINE  
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[PMID]:28625765
[Au] Autor:Lombard M; Hamdane D
[Ad] Endereço:Laboratoire de Chimie des Processus Biologiques, CNRS-UMR 8229, Collège De France, Université Pierre et marie Curie, 11 Place Marcelin Berthelot, 75231 Paris Cedex 05, France.
[Ti] Título:Flavin-dependent epitranscriptomic world.
[So] Source:Arch Biochem Biophys;632:28-40, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNAs molecules fulfill key roles in the expression and regulation of the genetic information stored within the DNA chromosomes. In addition to the four canonical bases, U, C, A and G, RNAs harbor various chemically modified derivatives which are generated post-transcriptionally by specific enzymes acting directly at the polymer level. More than one hundred naturally occurring modified nucleosides have been identified to date, the largest number of which is found in tRNAs and rRNA. This remarkable biochemical process produces widely diversified RNAs further expanding the functional repertoires of these nucleic acids. Interestingly, several RNA-modifying enzymes use a flavin bioorganic molecule as a coenzyme in RNA modification pathways. Some of these reactions are simple while others are extremely complex using challenging chemistry orchestrated by large flavoenzymatic systems. In this review, we summarize recent knowledges on the flavin-dependent RNA-modifying enzymes and discuss the relevance of their activity within a cellular context.
[Mh] Termos MeSH primário: Flavinas/metabolismo
Processamento Pós-Transcricional do RNA/fisiologia
RNA Ribossômico/metabolismo
RNA de Transferência/metabolismo
[Mh] Termos MeSH secundário: DNA/genética
DNA/metabolismo
Flavinas/genética
RNA Ribossômico/genética
RNA de Transferência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Flavins); 0 (RNA, Ribosomal); 9007-49-2 (DNA); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170620
[St] Status:MEDLINE


  8 / 2813 MEDLINE  
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[PMID]:28619619
[Au] Autor:Teufel R
[Ad] Endereço:ZBSA, Center for Biological Systems Analysis, University of Freiburg, 79104 Freiburg, Germany; Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany. Electronic address: robin.teufel@zbsa.de.
[Ti] Título:Flavin-catalyzed redox tailoring reactions in natural product biosynthesis.
[So] Source:Arch Biochem Biophys;632:20-27, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Natural products are distinct and often highly complex organic molecules that constitute not only an important drug source, but have also pushed the field of organic chemistry by providing intricate targets for total synthesis. How the astonishing structural diversity of natural products is enzymatically generated in biosynthetic pathways remains a challenging research area, which requires detailed and sophisticated approaches to elucidate the underlying catalytic mechanisms. Commonly, the diversification of precursor molecules into distinct natural products relies on the action of pathway-specific tailoring enzymes that catalyze, e.g., acylations, glycosylations, or redox reactions. This review highlights a selection of tailoring enzymes that employ riboflavin (vitamin B2)-derived cofactors (FAD and FMN) to facilitate unusual redox catalysis and steer the formation of complex natural product pharmacophores. Remarkably, several such recently reported flavin-dependent tailoring enzymes expand the classical paradigms of flavin biochemistry leading, e.g., to the discovery of the flavin-N5-oxide - a novel flavin redox state and oxygenating species.
[Mh] Termos MeSH primário: Flavinas/química
Espécies Reativas de Oxigênio/química
[Mh] Termos MeSH secundário: Catálise
Flavinas/metabolismo
Oxirredução
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Flavins); 0 (Reactive Oxygen Species)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE


  9 / 2813 MEDLINE  
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[PMID]:28608901
[Au] Autor:Lin CH; Lin TH; Pan TM
[Ad] Endereço:Department of Life Science, National Taitung University, No. 369, Sec. 2, University Rd., Taitung City, Taiwan.
[Ti] Título:Alleviation of metabolic syndrome by monascin and ankaflavin: the perspective of Monascus functional foods.
[So] Source:Food Funct;8(6):2102-2109, 2017 Jun 01.
[Is] ISSN:2042-650X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The metabolites of Monascus with multiple benefits are popular subjects for the development of functional foods. The yellow pigments, monascin and ankaflavin, which are the constituent metabolites of M. purpureus, M. pilosus and M. ruber, are becoming the focus of research on Monascus. Monascin and ankaflavin are azaphilone compounds with similar structures that exhibit multiple beneficial effects including anti-inflammation, anti-oxidation, anti-diabetes, immunomodulation, attenuation of Alzheimer's disease risk factor, and anti-tumorigenic effects. Monascin and ankaflavin not only possess pleiotropic bioactivities, but are also more potent than monacolin K in lowering lipid levels and have lower toxicity. Monascin and ankaflavin act as the activators of PPARγ agonist/Nrf-2 that subsequently ameliorate metabolic syndrome. Following the intensive exploration of Monascus bioactivities in recent years, the focus of research on Monascus-functional foods has shifted from whole fermented products/extracts to specific bioactive compounds. Therefore, the production of monascin and ankaflavin is an important topic with respect to Monascus-functional foods. Although several genomic studies have paved the way for understanding the production of secondary metabolites in Monascus, efforts are still required to effectively manipulate the biosynthesis of secondary metabolites with genetic engineering and/or culture techniques.
[Mh] Termos MeSH primário: Flavinas/metabolismo
Alimento Funcional/análise
Compostos Heterocíclicos com 3 Anéis/metabolismo
Síndrome Metabólica/dietoterapia
Monascus/química
[Mh] Termos MeSH secundário: Animais
Fermentação
Flavinas/química
Compostos Heterocíclicos com 3 Anéis/química
Seres Humanos
Síndrome Metabólica/genética
Síndrome Metabólica/metabolismo
Monascus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Flavins); 0 (Heterocyclic Compounds, 3-Ring); 0 (ankaflavin); W74D2M37FX (monascin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170614
[St] Status:MEDLINE
[do] DOI:10.1039/c7fo00406k


  10 / 2813 MEDLINE  
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[PMID]:28414427
[Au] Autor:Min D; Cheng L; Zhang F; Huang XN; Li DB; Liu DF; Lau TC; Mu Y; Yu HQ
[Ad] Endereço:CAS Key Laboratory of Urban Pollutant Conversion, Department of Chemistry, University of Science and Technology of China , Hefei, 230026, China.
[Ti] Título:Enhancing Extracellular Electron Transfer of Shewanella oneidensis MR-1 through Coupling Improved Flavin Synthesis and Metal-Reducing Conduit for Pollutant Degradation.
[So] Source:Environ Sci Technol;51(9):5082-5089, 2017 May 02.
[Is] ISSN:1520-5851
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dissimilatory metal reducing bacteria (DMRB) are capable of extracellular electron transfer (EET) to insoluble metal oxides, which are used as external electron acceptors by DMRB for their anaerobic respiration. The EET process has important contribution to environmental remediation mineral cycling, and bioelectrochemical systems. However, the low EET efficiency remains to be one of the major bottlenecks for its practical applications for pollutant degradation. In this work, Shewanella oneidensis MR-1, a model DMRB, was used to examine the feasibility of enhancing the EET and its biodegradation capacity through genetic engineering. A flavin biosynthesis gene cluster ribD-ribC-ribBA-ribE and metal-reducing conduit biosynthesis gene cluster mtrC-mtrA-mtrB were coexpressed in S. oneidensis MR-1. Compared to the control strain, the engineered strain was found to exhibit an improved EET capacity in microbial fuel cells and potentiostat-controlled electrochemical cells, with an increase in maximum current density by approximate 110% and 87%, respectively. The electrochemical impedance spectroscopy (EIS) analysis showed that the current increase correlated with the lower interfacial charge-transfer resistance of the engineered strain. Meanwhile, a three times more rapid removal rate of methyl orange by the engineered strain confirmed the improvement of its EET and biodegradation ability. Our results demonstrate that coupling of improved synthesis of mediators and metal-reducing conduits could be an efficient strategy to enhance EET in S. oneidensis MR-1, which is essential to the applications of DMRB for environmental remediation, wastewater treatment, and bioenergy recovery from wastes.
[Mh] Termos MeSH primário: Elétrons
Shewanella/metabolismo
[Mh] Termos MeSH secundário: Transporte de Elétrons
Flavinas
Metais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Flavins); 0 (Metals)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE
[do] DOI:10.1021/acs.est.6b04640



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